Structure of PDB 4v94 Chain f

Receptor sequence
>4v94f (length=538) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
SLQLLNPKAESLRRDAALKVNVTSAEGLQSVLETNLGPKGTLKMLVDGAG
NIKLTKDGKVLLTEMQIQSPTAVLIARAAAAQDEITGDGTTTVVCLVGEL
LRQAHRFIQEGVHPRIITDGFEIARKESMKFLDEFKISKTNLSNDREFLL
QVARSSLLTKVDADLTEVLTPIVTDAVLSVYDAQADNLDLHMVEIMQMQH
LSPKDTTFIKGLVLDHGGRHPDMPTRVKNAYVLILNVSLEYEKTEVNSGF
FYSSADQRDKLAASERKFVDAKLKKIIDLKNEVCGMDPDKGFVIINQKGI
DPMSLDVFAKHNILALRRAKRRNMERLQLVTGGEAQNSVEDLSPQILGFS
GLVYQETIGEEKFTYVTENTDPKSCTILIKGSTHYALAQTKDAVRDGLRA
VANVLKDKNIIPGAGAFYIALSRYLRSANMNKLGAKGKTKTGIEAFAEAL
LVIPKTLVKNSGFDPLDVLAMVEDELDDAQDSDETRYVGVDLNIGDSCDP
TIEGIWDSYRVLRNAITGATGIASNLLLCDELLRAGRS
3D structure
PDB4v94 The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT.
Chainf
Resolution3.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG f D89 T160 D88 T159
BS02 ADP f L37 G38 P39 D89 G90 T92 T93 T160 A415 L493 I506 L36 G37 P38 D88 G89 T91 T92 T159 A414 L492 I505
BS03 BEF f D58 G59 D89 T91 T92 K161 D57 G58 D88 T90 T91 K160
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding
GO:0051086 chaperone mediated protein folding independent of cofactor
Cellular Component
GO:0005737 cytoplasm
GO:0005832 chaperonin-containing T-complex

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Cellular Component
External links
PDB RCSB:4v94, PDBe:4v94, PDBj:4v94
PDBsum4v94
PubMed22503819
UniProtP39079|TCPZ_YEAST T-complex protein 1 subunit zeta (Gene Name=CCT6)

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